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Santa Cruz Biotechnology hrp conjugated secondary antibody
Treatment with SXR activators increases expression of p53 and p53 target genes . Total RNA was isolated from A) MCF-7 cells or B) ZR75-1 cells grown in the presence of 10 μM SXR activators rifampicin, anandamide, or clotrimazole (RIF, ANA or CLO) for 72 hours and 24 hours respectively. RNA was reverse transcribed and analyzed by QRT-PCR using primers for human p53, p21, BAX and PUMA. Data are depicted as average fold induction relative to solvent control in triplicates ± S.E.M. These results were replicated in at least three independent experiments. *represents P ≤ .05, **represents P ≤ .01 and # represents P ≤ .001 (by one-way ANOVA analysis). C) SXR activation causes p53 accumulation. Cell lysates made from C) MCF-7 and D) ZR-75-1 cells treated with SXR agonists (10 μM) or solvent controls for 72 and 24 hours respectively were subjected to Western blot analysis using p53 antibody (FL-393 <t>HRP,</t> Santa <t>Cruz</t> Inc.). Equal loading was confirmed by stripping and re-probing the same blot with an anti-GAPDH antibody. Camptothecin (CAMP) 24 hour treatment was used as a positive control for p53 induction. The chemiluminescent bands were acquired by Alpha Innotech Fluorchem SP imager (Alpha Innotech Inc., CA, USA) and analyzed by spot densitometry analysis using FluorChem AlphaEase FC software (Alpha Innotech). The experiment was done in duplicates and the numbers represent the average from two independent runs. Note that the gap in ANA lane of ZR-75-1 is because of gel tearing at the time of transferring.
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1) Product Images from "Activation of the steroid and xenobiotic receptor, SXR, induces apoptosis in breast cancer cells"

Article Title: Activation of the steroid and xenobiotic receptor, SXR, induces apoptosis in breast cancer cells

Journal: BMC Cancer

doi: 10.1186/1471-2407-9-3

Treatment with SXR activators increases expression of p53 and p53 target genes . Total RNA was isolated from A) MCF-7 cells or B) ZR75-1 cells grown in the presence of 10 μM SXR activators rifampicin, anandamide, or clotrimazole (RIF, ANA or CLO) for 72 hours and 24 hours respectively. RNA was reverse transcribed and analyzed by QRT-PCR using primers for human p53, p21, BAX and PUMA. Data are depicted as average fold induction relative to solvent control in triplicates ± S.E.M. These results were replicated in at least three independent experiments. *represents P ≤ .05, **represents P ≤ .01 and # represents P ≤ .001 (by one-way ANOVA analysis). C) SXR activation causes p53 accumulation. Cell lysates made from C) MCF-7 and D) ZR-75-1 cells treated with SXR agonists (10 μM) or solvent controls for 72 and 24 hours respectively were subjected to Western blot analysis using p53 antibody (FL-393 HRP, Santa Cruz Inc.). Equal loading was confirmed by stripping and re-probing the same blot with an anti-GAPDH antibody. Camptothecin (CAMP) 24 hour treatment was used as a positive control for p53 induction. The chemiluminescent bands were acquired by Alpha Innotech Fluorchem SP imager (Alpha Innotech Inc., CA, USA) and analyzed by spot densitometry analysis using FluorChem AlphaEase FC software (Alpha Innotech). The experiment was done in duplicates and the numbers represent the average from two independent runs. Note that the gap in ANA lane of ZR-75-1 is because of gel tearing at the time of transferring.
Figure Legend Snippet: Treatment with SXR activators increases expression of p53 and p53 target genes . Total RNA was isolated from A) MCF-7 cells or B) ZR75-1 cells grown in the presence of 10 μM SXR activators rifampicin, anandamide, or clotrimazole (RIF, ANA or CLO) for 72 hours and 24 hours respectively. RNA was reverse transcribed and analyzed by QRT-PCR using primers for human p53, p21, BAX and PUMA. Data are depicted as average fold induction relative to solvent control in triplicates ± S.E.M. These results were replicated in at least three independent experiments. *represents P ≤ .05, **represents P ≤ .01 and # represents P ≤ .001 (by one-way ANOVA analysis). C) SXR activation causes p53 accumulation. Cell lysates made from C) MCF-7 and D) ZR-75-1 cells treated with SXR agonists (10 μM) or solvent controls for 72 and 24 hours respectively were subjected to Western blot analysis using p53 antibody (FL-393 HRP, Santa Cruz Inc.). Equal loading was confirmed by stripping and re-probing the same blot with an anti-GAPDH antibody. Camptothecin (CAMP) 24 hour treatment was used as a positive control for p53 induction. The chemiluminescent bands were acquired by Alpha Innotech Fluorchem SP imager (Alpha Innotech Inc., CA, USA) and analyzed by spot densitometry analysis using FluorChem AlphaEase FC software (Alpha Innotech). The experiment was done in duplicates and the numbers represent the average from two independent runs. Note that the gap in ANA lane of ZR-75-1 is because of gel tearing at the time of transferring.

Techniques Used: Expressing, Isolation, Quantitative RT-PCR, Activation Assay, Western Blot, Stripping Membranes, Positive Control, Software, Transferring

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Blocking Assay:

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SDS-Gel:

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Incubation:

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Modification:

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Western Blot:

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High Performance Liquid Chromatography:

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Concentration Assay:

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Protease Inhibitor:

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Cell Culture:

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Sequencing:

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Affinity Purification:

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Binding Assay:

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Immunofluorescence:

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Isolation:

Article Title: Activation of the steroid and xenobiotic receptor, SXR, induces apoptosis in breast cancer cells
Article Snippet: Isolated IgG was affinity purified against this peptide prior to use. .. The primary antibody incubation was followed by 1 hr incubation at room temperature with HRP-conjugated secondary antibody (1:10,000; Santa Cruz Biotechnology Inc., USA).

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Polyacrylamide Gel Electrophoresis:

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SDS Page:

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Plasmid Preparation:

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Software:

Article Title: Activation of the steroid and xenobiotic receptor, SXR, induces apoptosis in breast cancer cells
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Electrophoresis:

Article Title: HCN1 and HCN2 Proteins Are Expressed in Cochlear Hair Cells
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Recombinant:

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Microscale Thermophoresis:

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Immunoprecipitation:

Article Title: HCN1 and HCN2 Proteins Are Expressed in Cochlear Hair Cells
Article Snippet: Paragraph title: Immunoprecipitation ... HRP-conjugated secondary antibodies (Santa Cruz Biotechnology) were diluted (1:6,000–1:10,000) in blocking solutions consisting of nonfat milk (1%) in PBST (plus 1% BSA for protocadherin 15 CD3) plus 2% serum corresponding to the species in which the secondary antibody was raised.

Two-Dimensional Gel Electrophoresis:

Article Title: A Rho GDP Dissociation Inhibitor Produced by Apoptotic T-Cells Inhibits Growth of Mycobacterium tuberculosis
Article Snippet: In some experiments, the supernatants were concentrated and 2D gel electrophoresis was performed, followed by LC-MS/MS analysis of differentially expressed proteins (Kendrick Laboratories, Madison, WI). .. After washing, the membranes were incubated with HRP-conjugated secondary Ab (Santa Cruz Biotechnology) and binding was detected by ECL (GE Healthcare).

Staining:

Article Title: SLC17A9 Protein Functions as a Lysosomal ATP Transporter and Regulates Cell Viability *
Article Snippet: The following primary antibodies were used for immunofluorescence staining and Western blotting: anti-SLC17A9 (MBL Co., Ltd., Nagoya, Japan), anti-Lamp1 (1D4B and H4A3, Developmental Studies Hybridoma Bank), anti-annexin V (Abcam), anti-GM130 (Abcam), anti-EEA1 (Abcam), anti-complex II (Invitrogen), and anti-GAPDH (Santa Cruz Biotechnology). .. HRP-conjugated secondary antibodies were purchased from Santa Cruz Biotechnology.

Chick Chorioallantoic Membrane Assay:

Article Title: Activation of the steroid and xenobiotic receptor, SXR, induces apoptosis in breast cancer cells
Article Snippet: The membranes were fixed in 0.2% glutaraldehyde in TBS for CaM protein before blocking in 3% BSA overnight followed by 1 hr incubation in mouse monoclonal CaM antibody (C-7055, Sigma-Aldrich, USA) at RT. .. The primary antibody incubation was followed by 1 hr incubation at room temperature with HRP-conjugated secondary antibody (1:10,000; Santa Cruz Biotechnology Inc., USA).

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    Santa Cruz Biotechnology hrp conjugated goat antirabbit igg
    SOCS3 expression in peripheral blood eosinophils from Th2 patients analyzed by immunohistochemical, immunofluorescence, and Western blot techniques. Eosinophils from asthmatic and NAEB patients within healthy controls were adhered to slides and incubated with peroxidase-conjugated goat <t>antirabbit</t> <t>IgG</t> against SOCS3 antibody ((b), (c), and (d)) or rabbit IgG as a control (a), and Texas Red conjugated goat antirabbit IgG against SOCS3 antibody ((f), (g), and (h)) or rabbit IgG as a control (e). The slides were observed by optical ((a), (b), (c), (d)) or confocal ((e), (f), (g) and (h)) microscopy. Western blot analysis of the cytosolic extract of purified eosinophils was achieved using antibody against SOCS3 (i). Lane 1: recombinant SOCS3 was loaded as a positive control; lane 2: eosinophil lysate from NAEB patients; lane 3: eosinophil lysate from healthy control patients; lane 4: isotype negative control. The picture is a representative example of 5 individuals, all displaying similar results. (j): SOCS3 bands were quantified by densitometry and corrected by actin expression; data are expressed as the mean ± SD, n = 5, * P
    Hrp Conjugated Goat Antirabbit Igg, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 80/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Santa Cruz Biotechnology hrp conjugated anti mouse igg antibody
    Expression of recombinant protein in ZYP-5052 medium. A) . Coomassie stained 12% SDS-PAGE of lysates shows proteins expressed in ZYP-5052 at 25°C at different incubation time. Equal culture densities (corresponding to 1 OD 600 cells) were analysed in each lane. Cells grown to saturation in PG, a non-inducing growth medium were loaded as control. Lane L: Protein marker; Lane C: Control; Lane 3 h-45 h: Induced samples at different incubation time, as indicated on top of each lane. B) . Western blot of expressed protein. Expressed protein was transferred to nitrocellulose membrane at 30 V overnight at 4°C. After blocking in 3% BSA, membrane was treated with mouse raised anti-His antibody (1 : 500) and <t>HRP-conjugated</t> anti-mouse <t>IgG</t> antibody and developed with DAB. Bold arrow denotes distinct band in induced sample corresponding to expressed protein of 25 kDa size. Control used is culture grown to saturation in PG medium. No expression is seen in control. Lane L: Protein marker; Lane C: Control; Lane 45 h: Sample processed 45 hr post incubation at 25°C.
    Hrp Conjugated Anti Mouse Igg Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Santa Cruz Biotechnology goat horseradish peroxidase hrp conjugated secondary anti mouse antibody
    <t>BtaE</t> localization. (A and C) Western blot analysis of whole-membrane fractions from B. suis (A) and E. coli pBBR btaE (C) was carried out. Membrane samples were submitted to a strong denaturing process. Samples were electrophoresed by SDS-PAGE and transferred to a PDVF membrane. Blots were incubated with anti-BtaE antisera and with anti-mouse <t>HRP-conjugated</t> secondary antibody and finally revealed using ECL Plus. On the right, a Coomassie blue pattern is shown as a loading control (ctrl). (B and D) Detection of BtaE (in red) on the B. suis surface (B) and on the E. coli pBBR btaE surface (D) by immunofluorescence of GFP-tagged bacteria. Cultures of GFP-labeled strains were fixed, incubated with anti-BtaE antibodies, and then probed with a CY3-conjugated donkey anti-mouse antibody preparation. Samples were observed with a Plan-Aprochromat 100×/1.4 oil DIC objective on a Zeiss LSM 5 Pascal confocal microscope.
    Goat Horseradish Peroxidase Hrp Conjugated Secondary Anti Mouse Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 78/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    82
    Santa Cruz Biotechnology anti pi3k p85 hrp conjugated secondary antibody
    The protein expression level of <t>PI3K</t> <t>p85.</t> Cells were treated with samples, or control for 72 h. Total protein was extracted for the analysis using Western blot. The signal of target protein in MCF-7 cells ( a , b ) and MDA-MB-231 cells ( c , d ) was detected and quantified using SuperSignal ELISA Pico Chemiluminescent Substrate. Data are presented as mean ± SD. * indicates a significant difference compared to the control ( p
    Anti Pi3k P85 Hrp Conjugated Secondary Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 82/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    SOCS3 expression in peripheral blood eosinophils from Th2 patients analyzed by immunohistochemical, immunofluorescence, and Western blot techniques. Eosinophils from asthmatic and NAEB patients within healthy controls were adhered to slides and incubated with peroxidase-conjugated goat antirabbit IgG against SOCS3 antibody ((b), (c), and (d)) or rabbit IgG as a control (a), and Texas Red conjugated goat antirabbit IgG against SOCS3 antibody ((f), (g), and (h)) or rabbit IgG as a control (e). The slides were observed by optical ((a), (b), (c), (d)) or confocal ((e), (f), (g) and (h)) microscopy. Western blot analysis of the cytosolic extract of purified eosinophils was achieved using antibody against SOCS3 (i). Lane 1: recombinant SOCS3 was loaded as a positive control; lane 2: eosinophil lysate from NAEB patients; lane 3: eosinophil lysate from healthy control patients; lane 4: isotype negative control. The picture is a representative example of 5 individuals, all displaying similar results. (j): SOCS3 bands were quantified by densitometry and corrected by actin expression; data are expressed as the mean ± SD, n = 5, * P

    Journal: Clinical and Developmental Immunology

    Article Title: Suppressors of Cytokine Signaling 3 Expression in Eosinophils: Regulation by PGE2 and Th2 Cytokines

    doi: 10.1155/2011/917015

    Figure Lengend Snippet: SOCS3 expression in peripheral blood eosinophils from Th2 patients analyzed by immunohistochemical, immunofluorescence, and Western blot techniques. Eosinophils from asthmatic and NAEB patients within healthy controls were adhered to slides and incubated with peroxidase-conjugated goat antirabbit IgG against SOCS3 antibody ((b), (c), and (d)) or rabbit IgG as a control (a), and Texas Red conjugated goat antirabbit IgG against SOCS3 antibody ((f), (g), and (h)) or rabbit IgG as a control (e). The slides were observed by optical ((a), (b), (c), (d)) or confocal ((e), (f), (g) and (h)) microscopy. Western blot analysis of the cytosolic extract of purified eosinophils was achieved using antibody against SOCS3 (i). Lane 1: recombinant SOCS3 was loaded as a positive control; lane 2: eosinophil lysate from NAEB patients; lane 3: eosinophil lysate from healthy control patients; lane 4: isotype negative control. The picture is a representative example of 5 individuals, all displaying similar results. (j): SOCS3 bands were quantified by densitometry and corrected by actin expression; data are expressed as the mean ± SD, n = 5, * P

    Article Snippet: The secondary antibody, HRP-conjugated goat antirabbit IgG (Santa Cruz Biotechnology, Inc.), was diluted 1 : 1000.

    Techniques: Expressing, Immunohistochemistry, Immunofluorescence, Western Blot, Incubation, Microscopy, Purification, Recombinant, Positive Control, Negative Control

    Expression of recombinant protein in ZYP-5052 medium. A) . Coomassie stained 12% SDS-PAGE of lysates shows proteins expressed in ZYP-5052 at 25°C at different incubation time. Equal culture densities (corresponding to 1 OD 600 cells) were analysed in each lane. Cells grown to saturation in PG, a non-inducing growth medium were loaded as control. Lane L: Protein marker; Lane C: Control; Lane 3 h-45 h: Induced samples at different incubation time, as indicated on top of each lane. B) . Western blot of expressed protein. Expressed protein was transferred to nitrocellulose membrane at 30 V overnight at 4°C. After blocking in 3% BSA, membrane was treated with mouse raised anti-His antibody (1 : 500) and HRP-conjugated anti-mouse IgG antibody and developed with DAB. Bold arrow denotes distinct band in induced sample corresponding to expressed protein of 25 kDa size. Control used is culture grown to saturation in PG medium. No expression is seen in control. Lane L: Protein marker; Lane C: Control; Lane 45 h: Sample processed 45 hr post incubation at 25°C.

    Journal: Virology Journal

    Article Title: Cloning and expression of N22 region of Torque Teno virus (TTV) genome and use of peptide in developing immunoassay for TTV antibodies

    doi: 10.1186/1743-422X-11-96

    Figure Lengend Snippet: Expression of recombinant protein in ZYP-5052 medium. A) . Coomassie stained 12% SDS-PAGE of lysates shows proteins expressed in ZYP-5052 at 25°C at different incubation time. Equal culture densities (corresponding to 1 OD 600 cells) were analysed in each lane. Cells grown to saturation in PG, a non-inducing growth medium were loaded as control. Lane L: Protein marker; Lane C: Control; Lane 3 h-45 h: Induced samples at different incubation time, as indicated on top of each lane. B) . Western blot of expressed protein. Expressed protein was transferred to nitrocellulose membrane at 30 V overnight at 4°C. After blocking in 3% BSA, membrane was treated with mouse raised anti-His antibody (1 : 500) and HRP-conjugated anti-mouse IgG antibody and developed with DAB. Bold arrow denotes distinct band in induced sample corresponding to expressed protein of 25 kDa size. Control used is culture grown to saturation in PG medium. No expression is seen in control. Lane L: Protein marker; Lane C: Control; Lane 45 h: Sample processed 45 hr post incubation at 25°C.

    Article Snippet: For immunodetection of the His fusion proteins, the primary antibody used was His probe (H-3) mouse monoclonal IgG (1 : 500; Santa Cruz Biotechnology, USA) and the secondary antibody was HRP-conjugated anti-mouse IgG antibody (1 : 2000; Santa Cruz Biotechnology, USA).

    Techniques: Expressing, Recombinant, Staining, SDS Page, Incubation, Marker, Western Blot, Blocking Assay

    BtaE localization. (A and C) Western blot analysis of whole-membrane fractions from B. suis (A) and E. coli pBBR btaE (C) was carried out. Membrane samples were submitted to a strong denaturing process. Samples were electrophoresed by SDS-PAGE and transferred to a PDVF membrane. Blots were incubated with anti-BtaE antisera and with anti-mouse HRP-conjugated secondary antibody and finally revealed using ECL Plus. On the right, a Coomassie blue pattern is shown as a loading control (ctrl). (B and D) Detection of BtaE (in red) on the B. suis surface (B) and on the E. coli pBBR btaE surface (D) by immunofluorescence of GFP-tagged bacteria. Cultures of GFP-labeled strains were fixed, incubated with anti-BtaE antibodies, and then probed with a CY3-conjugated donkey anti-mouse antibody preparation. Samples were observed with a Plan-Aprochromat 100×/1.4 oil DIC objective on a Zeiss LSM 5 Pascal confocal microscope.

    Journal: Infection and Immunity

    Article Title: BtaE, an Adhesin That Belongs to the Trimeric Autotransporter Family, Is Required for Full Virulence and Defines a Specific Adhesive Pole of Brucella suis

    doi: 10.1128/IAI.01241-12

    Figure Lengend Snippet: BtaE localization. (A and C) Western blot analysis of whole-membrane fractions from B. suis (A) and E. coli pBBR btaE (C) was carried out. Membrane samples were submitted to a strong denaturing process. Samples were electrophoresed by SDS-PAGE and transferred to a PDVF membrane. Blots were incubated with anti-BtaE antisera and with anti-mouse HRP-conjugated secondary antibody and finally revealed using ECL Plus. On the right, a Coomassie blue pattern is shown as a loading control (ctrl). (B and D) Detection of BtaE (in red) on the B. suis surface (B) and on the E. coli pBBR btaE surface (D) by immunofluorescence of GFP-tagged bacteria. Cultures of GFP-labeled strains were fixed, incubated with anti-BtaE antibodies, and then probed with a CY3-conjugated donkey anti-mouse antibody preparation. Samples were observed with a Plan-Aprochromat 100×/1.4 oil DIC objective on a Zeiss LSM 5 Pascal confocal microscope.

    Article Snippet: Blots were probed with polyclonal mouse anti-BtaE serum (1:8,000) and a goat horseradish peroxidase (HRP)-conjugated secondary anti-mouse antibody (1:30,000; Santa Cruz) and then revealed using ECL Plus (Amersham).

    Techniques: Western Blot, SDS Page, Incubation, Immunofluorescence, Labeling, Microscopy

    The protein expression level of PI3K p85. Cells were treated with samples, or control for 72 h. Total protein was extracted for the analysis using Western blot. The signal of target protein in MCF-7 cells ( a , b ) and MDA-MB-231 cells ( c , d ) was detected and quantified using SuperSignal ELISA Pico Chemiluminescent Substrate. Data are presented as mean ± SD. * indicates a significant difference compared to the control ( p

    Journal: Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry

    Article Title: Synergistic Effect of Bioactive Anticarcinogens from Soybean on Anti-Proliferative Activity in MDA-MB-231 and MCF-7 Human Breast Cancer Cells In Vitro

    doi: 10.3390/molecules23071557

    Figure Lengend Snippet: The protein expression level of PI3K p85. Cells were treated with samples, or control for 72 h. Total protein was extracted for the analysis using Western blot. The signal of target protein in MCF-7 cells ( a , b ) and MDA-MB-231 cells ( c , d ) was detected and quantified using SuperSignal ELISA Pico Chemiluminescent Substrate. Data are presented as mean ± SD. * indicates a significant difference compared to the control ( p

    Article Snippet: Anti-PI3K p85 HRP-conjugated secondary antibody (Santa Cruz Biotechnology, Santa Cruz, CA, USA) were used.

    Techniques: Expressing, Western Blot, Multiple Displacement Amplification, Enzyme-linked Immunosorbent Assay